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Q12874

- SF3A3_HUMAN

UniProt

Q12874 - SF3A3_HUMAN

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Protein

Splicing factor 3A subunit 3

Gene

SF3A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri406 – 43732Matrin-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA 3'-splice site recognition Source: HGNC
  3. mRNA processing Source: HGNC
  4. mRNA splicing, via spliceosome Source: UniProtKB
  5. RNA splicing Source: Reactome
  6. RNA splicing, via transesterification reactions Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor 3A subunit 3
Alternative name(s):
SF3a60
Spliceosome-associated protein 61
Short name:
SAP 61
Gene namesi
Name:SF3A3
Synonyms:SAP61
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10767. SF3A3.

Subcellular locationi

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. spliceosomal complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35685.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Splicing factor 3A subunit 3PRO_0000174318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Glycosylationi119 – 1191N-linked (GlcNAc...)1 Publication
Modified residuei299 – 2991Phosphoserine1 Publication
Modified residuei365 – 3651Phosphoserine3 Publications
Modified residuei367 – 3671Phosphoserine3 Publications
Modified residuei369 – 3691Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ12874.
PaxDbiQ12874.
PeptideAtlasiQ12874.
PRIDEiQ12874.

PTM databases

PhosphoSiteiQ12874.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ12874.
CleanExiHS_SF3A3.
GenevestigatoriQ12874.

Organism-specific databases

HPAiHPA032054.

Interactioni

Subunit structurei

Identified in the spliceosome C complex. Component of splicing factor SF3A which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts with SF3A1, through its N-terminal region.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPB1P047922EBI-1051880,EBI-352682
ORFQ9Q2G43EBI-1051880,EBI-6248094From a different organism.
SF3A1Q154592EBI-1051880,EBI-1054743

Protein-protein interaction databases

BioGridi116146. 67 interactions.
DIPiDIP-882N.
IntActiQ12874. 15 interactions.
MINTiMINT-1467744.
STRINGi9606.ENSP00000362110.

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi80 – 9617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DT7NMR-A71-107[»]
ProteinModelPortaliQ12874.
SMRiQ12874. Positions 71-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12874.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi354 – 3629Poly-Glu

Sequence similaritiesi

Belongs to the SF3A3 family.Curated
Contains 1 matrin-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri406 – 43732Matrin-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5188.
GeneTreeiENSGT00530000063402.
HOGENOMiHOG000160935.
HOVERGENiHBG054452.
InParanoidiQ12874.
KOiK12827.
OMAiYLDLHEC.
OrthoDBiEOG77HDDF.
PhylomeDBiQ12874.
TreeFamiTF315227.

Family and domain databases

InterProiIPR024598. DUF3449.
IPR021966. SF3a60_bindingd.
IPR015880. Znf_C2H2-like.
IPR000690. Znf_C2H2_matrin.
[Graphical view]
PfamiPF11931. DUF3449. 1 hit.
PF12108. SF3a60_bindingd. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS50171. ZF_MATRIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12874-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
METILEQQRR YHEEKERLMD VMAKEMLTKK STLRDQINSD HRTRAMQDRY
60 70 80 90 100
MEVSGNLRDL YDDKDGLRKE ELNAISGPNE FAEFYNRLKQ IKEFHRKHPN
110 120 130 140 150
EICVPMSVEF EELLKARENP SEEAQNLVEF TDEEGYGRYL DLHDCYLKYI
160 170 180 190 200
NLKASEKLDY ITYLSIFDQL FDIPKERKNA EYKRYLEMLL EYLQDYTDRV
210 220 230 240 250
KPLQDQNELF GKIQAEFEKK WENGTFPGWP KETSSALTHA GAHLDLSAFS
260 270 280 290 300
SWEELASLGL DRLKSALLAL GLKCGGTLEE RAQRLFSTKG KSLESLDTSL
310 320 330 340 350
FAKNPKSKGT KRDTERNKDI AFLEAQIYEY VEILGEQRHL THENVQRKQA
360 370 380 390 400
RTGEEREEEE EEQISESESE DEENEIIYNP KNLPLGWDGK PIPYWLYKLH
410 420 430 440 450
GLNINYNCEI CGNYTYRGPK AFQRHFAEWR HAHGMRCLGI PNTAHFANVT
460 470 480 490 500
QIEDAVSLWA KLKLQKASER WQPDTEEEYE DSSGNVVNKK TYEDLKRQGL

L
Length:501
Mass (Da):58,849
Last modified:November 1, 1996 - v1
Checksum:i6E6F6EA17777E1E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761E → G in CAA57388. (PubMed:7816610)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08815 mRNA. Translation: AAA19625.1.
X81789 mRNA. Translation: CAA57388.1.
AL603790 Genomic DNA. Translation: CAH69930.1.
CH471059 Genomic DNA. Translation: EAX07304.1.
CH471059 Genomic DNA. Translation: EAX07305.1.
BC002395 mRNA. Translation: AAH02395.1.
BC011523 mRNA. Translation: AAH11523.1.
CCDSiCCDS428.1.
PIRiA55749.
RefSeqiNP_006793.1. NM_006802.2.
UniGeneiHs.77897.

Genome annotation databases

EnsembliENST00000373019; ENSP00000362110; ENSG00000183431.
GeneIDi10946.
KEGGihsa:10946.
UCSCiuc001cci.3. human.

Polymorphism databases

DMDMi17380310.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08815 mRNA. Translation: AAA19625.1 .
X81789 mRNA. Translation: CAA57388.1 .
AL603790 Genomic DNA. Translation: CAH69930.1 .
CH471059 Genomic DNA. Translation: EAX07304.1 .
CH471059 Genomic DNA. Translation: EAX07305.1 .
BC002395 mRNA. Translation: AAH02395.1 .
BC011523 mRNA. Translation: AAH11523.1 .
CCDSi CCDS428.1.
PIRi A55749.
RefSeqi NP_006793.1. NM_006802.2.
UniGenei Hs.77897.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DT7 NMR - A 71-107 [» ]
ProteinModelPortali Q12874.
SMRi Q12874. Positions 71-107.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116146. 67 interactions.
DIPi DIP-882N.
IntActi Q12874. 15 interactions.
MINTi MINT-1467744.
STRINGi 9606.ENSP00000362110.

PTM databases

PhosphoSitei Q12874.

Polymorphism databases

DMDMi 17380310.

Proteomic databases

MaxQBi Q12874.
PaxDbi Q12874.
PeptideAtlasi Q12874.
PRIDEi Q12874.

Protocols and materials databases

DNASUi 10946.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373019 ; ENSP00000362110 ; ENSG00000183431 .
GeneIDi 10946.
KEGGi hsa:10946.
UCSCi uc001cci.3. human.

Organism-specific databases

CTDi 10946.
GeneCardsi GC01M038422.
HGNCi HGNC:10767. SF3A3.
HPAi HPA032054.
MIMi 605596. gene.
neXtProti NX_Q12874.
PharmGKBi PA35685.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5188.
GeneTreei ENSGT00530000063402.
HOGENOMi HOG000160935.
HOVERGENi HBG054452.
InParanoidi Q12874.
KOi K12827.
OMAi YLDLHEC.
OrthoDBi EOG77HDDF.
PhylomeDBi Q12874.
TreeFami TF315227.

Enzyme and pathway databases

Reactomei REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi SF3A3. human.
EvolutionaryTracei Q12874.
GeneWikii SF3A3.
GenomeRNAii 10946.
NextBioi 41589.
PROi Q12874.
SOURCEi Search...

Gene expression databases

Bgeei Q12874.
CleanExi HS_SF3A3.
Genevestigatori Q12874.

Family and domain databases

InterProi IPR024598. DUF3449.
IPR021966. SF3a60_bindingd.
IPR015880. Znf_C2H2-like.
IPR000690. Znf_C2H2_matrin.
[Graphical view ]
Pfami PF11931. DUF3449. 1 hit.
PF12108. SF3a60_bindingd. 1 hit.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
PROSITEi PS50171. ZF_MATRIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Specific protein-protein interactions between the essential mammalian spliceosome-associated proteins SAP 61 and SAP 114."
    Chiara M.D., Champion-Arnaud P., Buvoli M., Nadal-Ginard B., Reed R.
    Proc. Natl. Acad. Sci. U.S.A. 91:6403-6407(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cervix adenocarcinoma.
  2. "Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: the conserved zinc finger-like motif is functionally exchangeable in vivo."
    Kraemer A., Legrain P., Mulhauser F., Groening K., Brosi R., Bilbe G.
    Nucleic Acids Res. 22:5223-5228(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Cervix adenocarcinoma.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye and Lung.
  6. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-9; 265-273 AND 292-303, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  7. "Functional association of U2 snRNP with the ATP-independent spliceosomal complex E."
    Das R., Zhou Z., Reed R.
    Mol. Cell 5:779-787(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE SPLICEOSOME.
  8. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119.
    Tissue: Liver.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-365; SER-367 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP."
    Kuwasako K., He F., Inoue M., Tanaka A., Sugano S., Guntert P., Muto Y., Yokoyama S.
    Structure 14:1677-1689(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 71-107 IN COMPLEX WITH SF3A1, SUBUNIT.

Entry informationi

Entry nameiSF3A3_HUMAN
AccessioniPrimary (citable) accession number: Q12874
Secondary accession number(s): D3DPT5, Q15460, Q5VT87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3